7rd6

<table><tr><td colspan='2'>[[7rd6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RD6 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/P-type_phospholipid_transporter P-type phospholipid transporter], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.6.2.1 7.6.2.1] </span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/ATC7_YEAST ATC7_YEAST]] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Leads to neomycin-resistance when overexpressed. Required for traffic between late Golgi and early endosomes.<ref>PMID:15314152</ref>

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== Publication Abstract from PubMed ==

P4 ATPases are lipid flippases that are phylogenetically grouped into P4A, P4B and P4C clades. The P4A ATPases are heterodimers composed of a catalytic alpha-subunit and accessory beta-subunit, and the structures of several heterodimeric flippases have been reported. The S. cerevisiae Neo1 and its orthologs represent the P4B ATPases, which function as monomeric flippases without a beta-subunit. It has been unclear whether monomeric flippases retain the architecture and transport mechanism of the dimeric flippases. Here we report the structure of a P4B ATPase, Neo1, in its E1-ATP, E2P-transition, and E2P states. The structure reveals a conserved architecture as well as highly similar functional intermediate states relative to dimeric flippases. Consistently, structure-guided mutagenesis of residues in the proposed substrate translocation path disrupted Neo1's ability to establish membrane asymmetry. These observations indicate that evolutionarily distant P4 ATPases use a structurally conserved mechanism for substrate transport.

Structural basis of the P4B ATPase lipid flippase activity.,Bai L, Jain BK, You Q, Duan HD, Takar M, Graham TR, Li H Nat Commun. 2021 Oct 13;12(1):5963. doi: 10.1038/s41467-021-26273-0. PMID:34645814<ref>PMID:34645814</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bai, L]]

[[Category: Duan, H D]]

[[Category: Graham, T R]]

[[Category: Jain, B K]]

[[Category: Li, H]]

[[Category: You, Q]]

[[Category: Translocase]]